Abstract
Organisms use molecular chaperones to combat the unfolding and aggregation of proteins. While protein chaperones have been widely studied, here we demonstrate that DNA and RNA exhibit potent chaperone activity in vitro. Nucleic acids suppress the aggregation of classic chaperone substrates up to 300-fold more effectively than the protein chaperone GroEL. Additionally, RNA cooperates with the DnaK chaperone system to refold purified luciferase. Our findings reveal a possible new role for nucleic acids within the cell: that nucleic acids directly participate in maintaining proteostasis by preventing protein aggregation.
Highlights
One of the major impacts of cellular stress is the unfolding and aggregation of proteins
The previously observed chaperone-like properties of ribosomal RNA, and the consideration that nucleic acids are chemically similar to polyphosphate, we decided to test whether nucleic acids might generally act as chaperones
The chaperone activity did not depend on the buffer, as the activity persisted in both HEPES (Figure 1B) and 10 mM phosphate buffer (Figure 1C), as well as other buffers (Supplementary Figures S1 and S2). dsDNA displayed similar activity upon citrate synthase (CS) that had been denatured in 6 M guanidinium HCl (Figure 1D)
Summary
One of the major impacts of cellular stress is the unfolding and aggregation of proteins. To deal with this problem, cells mobilize molecular chaperones, which bind to misfolded proteins and prevent their aggregation. DNA, RNA and polyanions, including heparin, have been shown to accelerate the folding of a variety of nucleic acid binding proteins up to 30-fold [4]. This acceleration is likely in part due to the stabilizing influence of specific binding [5]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
